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Database: UniProt
Entry: A0A132AAN9_SARSC
LinkDB: A0A132AAN9_SARSC
Original site: A0A132AAN9_SARSC 
ID   A0A132AAN9_SARSC        Unreviewed;       330 AA.
AC   A0A132AAN9;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   22-NOV-2017, entry version 14.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|RuleBase:RU364074};
DE            EC=1.2.4.1 {ECO:0000256|RuleBase:RU364074};
GN   ORFNames=QR98_0064620 {ECO:0000313|EMBL:KPM07949.1};
OS   Sarcoptes scabiei (Itch mite) (Acarus scabiei).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Acari; Acariformes; Sarcoptiformes; Astigmata; Psoroptidia;
OC   Sarcoptoidea; Sarcoptidae; Sarcoptinae; Sarcoptes.
OX   NCBI_TaxID=52283 {ECO:0000313|EMBL:KPM07949.1, ECO:0000313|Proteomes:UP000070412};
RN   [1] {ECO:0000313|EMBL:KPM07949.1, ECO:0000313|Proteomes:UP000070412, ECO:0000313|VectorBase:SSCA005907-PA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Arlian Lab {ECO:0000313|EMBL:KPM07949.1};
RX   PubMed=26555130; DOI=10.1186/s13071-015-1198-2;
RA   Rider S.D.Jr., Morgan M.S., Arlian L.G.;
RT   "Draft genome of the scabies mite.";
RL   Parasit. Vectors 8:585-585(2015).
RN   [2] {ECO:0000313|VectorBase:SSCA005907-PA}
RP   IDENTIFICATION.
RG   VectorBase;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO2.
CC       {ECO:0000256|RuleBase:RU364074}.
CC   -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue
CC       acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
CC       {ECO:0000256|RuleBase:RU364074}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|RuleBase:RU364074};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|RuleBase:RU364074}.
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DR   EMBL; JXLN01012044; KPM07949.1; -; Genomic_DNA.
DR   EnsemblMetazoa; SSCA005907-RA; SSCA005907-PA; SSCA005907.
DR   VectorBase; SSCA005907-RA; SSCA005907-PA; SSCA005907.
DR   OMA; QEMTRDP; -.
DR   Proteomes; UP000070412; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.920; -; 1.
DR   InterPro; IPR027110; PDHB.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   PANTHER; PTHR11624:SF94; PTHR11624:SF94; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
DR   SUPFAM; SSF52922; SSF52922; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000070412};
KW   Glycolysis {ECO:0000256|RuleBase:RU364074};
KW   Mitochondrion {ECO:0000256|RuleBase:RU364074};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364074};
KW   Pyruvate {ECO:0000256|RuleBase:RU364074, ECO:0000313|EMBL:KPM07949.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070412};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU364074};
KW   Transit peptide {ECO:0000256|RuleBase:RU364074}.
FT   DOMAIN        4    177       Transket_pyr. {ECO:0000259|SMART:
FT                                SM00861}.
SQ   SEQUENCE   330 AA;  36013 MW;  89CD317E3C55A1A2 CRC64;
     MTKRKNADAI ALDEELERDE SVFILGEEVA QYDGAYKVTK GLWRKYGDQR VIDTPITEMG
     FAGIAVGAAF YGLKPVCEFM TFNFAMQAID QIINSAAKTH YMSAGRIAVP IVFRGPNGAA
     AGVAAQHSQC YAAWYSHCPG LKVLAPYSAE DAKGLLKSAI RDPDPIIFLE NEILYGTSFE
     VSDDVLSKEF LLPIGKAKIE RRGEHVTICA YSRAIETSLE AAEILAASCN IELEVINLRT
     IRPLDFQTIA DSVIKTNHLI TVEQGWPQSG VGAEICAQIV ESPIFDYLDA PVVRITGADV
     PMPYARTLEI NAIPQPGNIV AAVKQMLNIN
//
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